Hau, Jann-Louis ; Schleicher, Lena ; Herdan, Sebastian ; Simon, Jörg ; Seifert, Jana ; Fritz, Günter ; Steuber, Julia (2024)
Functionality of the Na+‑translocating NADH:quinone oxidoreductase and quinol:fumarate reductase from Prevotella bryantii inferred from homology modeling.
In: Archives of microbiology, 206 (1)
doi: 10.1007/s00203-023-03769-5
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
Members of the family Prevotellaceae are Gram-negative, obligate anaerobic bacteria found in animal and human microbiota. In Prevotella bryantii, the Na-translocating NADH:quinone oxidoreductase (NQR) and quinol:fumarate reductase (QFR) interact using menaquinone as electron carrier, catalyzing NADH:fumarate oxidoreduction. P. bryantii NQR establishes a sodium-motive force, whereas P. bryantii QFR does not contribute to membrane energization. To elucidate the possible mode of function, we present 3D structural models of NQR and QFR from P. bryantii to predict cofactor-binding sites, electron transfer routes and interaction with substrates. Molecular docking reveals the proposed mode of menaquinone binding to the quinone site of subunit NqrB of P. bryantii NQR. A comparison of the 3D model of P. bryantii QFR with experimentally determined structures suggests alternative pathways for transmembrane proton transport in this type of QFR. Our findings are relevant for NADH-dependent succinate formation in anaerobic bacteria which operate both NQR and QFR.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2024 |
| Autor(en): | Hau, Jann-Louis ; Schleicher, Lena ; Herdan, Sebastian ; Simon, Jörg ; Seifert, Jana ; Fritz, Günter ; Steuber, Julia |
| Art des Eintrags: | Bibliographie |
| Titel: | Functionality of the Na+‑translocating NADH:quinone oxidoreductase and quinol:fumarate reductase from Prevotella bryantii inferred from homology modeling |
| Sprache: | Englisch |
| Publikationsjahr: | Januar 2024 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Archives of microbiology |
| Jahrgang/Volume einer Zeitschrift: | 206 |
| (Heft-)Nummer: | 1 |
| DOI: | 10.1007/s00203-023-03769-5 |
| Kurzbeschreibung (Abstract): | Members of the family Prevotellaceae are Gram-negative, obligate anaerobic bacteria found in animal and human microbiota. In Prevotella bryantii, the Na-translocating NADH:quinone oxidoreductase (NQR) and quinol:fumarate reductase (QFR) interact using menaquinone as electron carrier, catalyzing NADH:fumarate oxidoreduction. P. bryantii NQR establishes a sodium-motive force, whereas P. bryantii QFR does not contribute to membrane energization. To elucidate the possible mode of function, we present 3D structural models of NQR and QFR from P. bryantii to predict cofactor-binding sites, electron transfer routes and interaction with substrates. Molecular docking reveals the proposed mode of menaquinone binding to the quinone site of subunit NqrB of P. bryantii NQR. A comparison of the 3D model of P. bryantii QFR with experimentally determined structures suggests alternative pathways for transmembrane proton transport in this type of QFR. Our findings are relevant for NADH-dependent succinate formation in anaerobic bacteria which operate both NQR and QFR. |
| ID-Nummer: | pmid:38127130 |
| Zusätzliche Informationen: | Published Online: 21.12.2023 |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie 10 Fachbereich Biologie > Microbial Energy Conversion and Biotechnology |
| Hinterlegungsdatum: | 28 Dez 2023 09:39 |
| Letzte Änderung: | 28 Dez 2023 09:48 |
| PPN: | 514294884 |
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